RHAD_ENT38
ID RHAD_ENT38 Reviewed; 276 AA.
AC A4WG94;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Rhamnulose-1-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00770};
DE EC=4.1.2.19 {ECO:0000255|HAMAP-Rule:MF_00770};
GN Name=rhaD {ECO:0000255|HAMAP-Rule:MF_00770}; OrderedLocusNames=Ent638_4069;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
CC -!- FUNCTION: Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate
CC to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
CC {ECO:0000255|HAMAP-Rule:MF_00770}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-rhamnulose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone
CC phosphate; Xref=Rhea:RHEA:19689, ChEBI:CHEBI:18041,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:58313; EC=4.1.2.19;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00770};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00770};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00770};
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC phosphate from L-rhamnose: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00770}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00770}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00770}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. RhaD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00770}.
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DR EMBL; CP000653; ABP62724.1; -; Genomic_DNA.
DR RefSeq; WP_015961028.1; NC_009436.1.
DR AlphaFoldDB; A4WG94; -.
DR SMR; A4WG94; -.
DR STRING; 399742.Ent638_4069; -.
DR EnsemblBacteria; ABP62724; ABP62724; Ent638_4069.
DR KEGG; ent:Ent638_4069; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_076831_0_0_6; -.
DR OMA; SHFMSHI; -.
DR OrthoDB; 599627at2; -.
DR UniPathway; UPA00541; UER00603.
DR Proteomes; UP000000230; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008994; F:rhamnulose-1-phosphate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.225.10; -; 1.
DR HAMAP; MF_00770; RhaD; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR013447; Rhamnulose-1-P_Aldolase.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR TIGRFAMs; TIGR02624; rhamnu_1P_ald; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Metal-binding; Rhamnose metabolism; Zinc.
FT CHAIN 1..276
FT /note="Rhamnulose-1-phosphate aldolase"
FT /id="PRO_1000062240"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
SQ SEQUENCE 276 AA; 30367 MW; A2575A809B954C3E CRC64;
MQTITNAWFV QGMIKATTDA WLKGWDERNG GNLTLRLDNA DIAPFEADFH QKPRYIALSQ
PMPLLANTAF IVTGSGKFFR NVQLDPTANL GVVKVDSDGA GYHILWGLTN EAVPTSELPA
HFLSHCERIK ATDGKDRVIM HCHATNLIAL TYVLENDSAF ITRKLWEGST ECLVVFPDGV
GILPWMVPGT DEIGQATAQD MQKHSLVLWP FHGVFGSGPT LDEAFGLIDT AEKSAEVLVK
VYSMGGMKQT ITQEELIALG KRFGVTPMKS ALELYK